Inhibition of Tyrosine Protein Phosphatases from Muscle and Spleen by Nucleic Acids and Polyanions

  • C. Stader
  • S. Dierig
  • N. Tidow
  • S. Kirsch
  • H. W. Hofer
Conference paper
Part of the NATO ASI Series book series (volume 56)

Abstract

The reversion of tyrosine phosphorylation is potentially involved in the regulation of the cell cycle and signal transduction (cf. to the contributions by E. Fischer and G. Draetta, this volume). Structural relationship was detected between a 38 kDa protein tyrosine phosphatase (PTP) isolated from human placenta (PTP-1B, Tonks et al., 1988) and the catalytic domains of membrane proteins like CD45 (Tonks et al., 1990), LAR (Streuli et al., 1988), and LCP (Matthews et al., 1990) which possess tyrosine phosphatase activity. Clones encoding for a major soluble PTP of Mr ≈ 50,000 have been obtained from human and rat cDNA libraries (Chernoff et al., 1990; Brown- Shimer et al., 1990; Guan et al., 1990). These clones included the complete code for PTP-1B indicating that PTP-1B was a proteolytic fragment of a larger precursor. We isolated PTPs from the cytosolic fraction of porcine spleen (designated PTP-S) and two soluble enzymes (designated PTP-M1 and PTP-M2) from rat muscle and compared their properties with respect to the inhibition by various polyanions.

Keywords

Migration Filtration Tyrosine Heparin Trypsin 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • C. Stader
    • 1
  • S. Dierig
    • 1
  • N. Tidow
    • 1
  • S. Kirsch
    • 1
  • H. W. Hofer
    • 1
  1. 1.Faculty of BiologyUniversity of KonstanzKonstanzGermany

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